Evidence map›Paper›PMID 27070572›Full record

ArticleInternational journal of molecular sciences2016

SAAFEC: Predicting the Effect of Single Point Mutations on Protein Folding Free Energy Using a Knowledge-Modified MM/PBSA Approach.

Ivan Getov, Marharyta Petukh, Emil Alexov

Abstract read
In one paragraph

Article in International journal of molecular sciences, 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 45 papers.

0numbers the graph read from it
0cells of the map it votes in
45citing papers in PubMed
–field-weighted citation impact
1 · What the graph read from it

What it found

Each row is one number read from the abstract, on the scale the paper reported it, with its interval. Left of the dashed line favours the treatment, right favours the comparator. Under each row is the sentence it came from. New to these charts? A ten-minute tutorial.

The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.

2 · The registry

The trial behind it

Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.

Neither the registry nor the abstract names a trial number. If this is a trial report, that itself is worth knowing.

3 · Its place in the literature

Who cites it

45 citing papers in PubMed.

  1. Article
  2. Article
  3. Review
  4. Topological deep learning based deep mutational scanning.Computers in biology and medicine · 2023
    Article
  5. Article
  6. Article
  7. Article
  8. Article
  9. Article
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  14. Article
  15. Decoding Asymptomatic COVID-19 Infection and Transmission.The journal of physical chemistry letters · 2020
    Review
  16. Article
  17. Article
  18. Article
  19. Article
  20. Article
4 · The record

Corrections and comments

PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.

5 · Who and what money

Authors and funding

3 authors.

Ivan GetovComputational Biophysics and Bioinformatics, Physics Department, Clemson University, Clemson, SC 29634, USA. igetov@clemson.edu.
Marharyta PetukhComputational Biophysics and Bioinformatics, Physics Department, Clemson University, Clemson, SC 29634, USA. mpetukh@clemson.edu.
Emil AlexovComputational Biophysics and Bioinformatics, Physics Department, Clemson University, Clemson, SC 29634, USA. ealexov@clemson.edu.

Funding

New Generation DelPhi: large systems and beyond electrostaticsR01GM093937 · NIGMS · CLEMSON UNIVERSITY · PI ALEXOV, EMIL GEORGIEV · 2010 to 2023
$4.3M
NIGMS NIH HHS R01 GM093937
6 · The paper itself

Abstract

unlabelledFolding free energy is an important biophysical characteristic of proteins that reflects the overall stability of the 3D structure of macromolecules. Changes in the amino acid sequence, naturally occurring or made in vitro, may affect the stability of the corresponding protein and thus could be associated with disease. Several approaches that predict the changes of the folding free energy caused by mutations have been proposed, but there is no method that is clearly superior to the others. The optimal goal is not only to accurately predict the folding free energy changes, but also to characterize the structural changes induced by mutations and the physical nature of the predicted folding free energy changes. Here we report a new method to predict the Single Amino Acid Folding free Energy Changes (SAAFEC) based on a knowledge-modified Molecular Mechanics Poisson-Boltzmann (MM/PBSA) approach. The method is comprised of two main components: a MM/PBSA component and a set of knowledge based terms delivered from a statistical study of the biophysical characteristics of proteins. The predictor utilizes a multiple linear regression model with weighted coefficients of various terms optimized against a set of experimental data. The aforementioned approach yields a correlation coefficient of 0.65 when benchmarked against 983 cases from 42 proteins in the ProTherm database. AVAILABILITY: the webserver can be accessed via http://compbio.clemson.edu/SAAFEC/.

Indexed as

Point MutationProtein FoldingThermodynamicsComputer SimulationDatabases, ProteinModels, BiologicalProteinsProteinsenergy calculationfolding free energymissense mutationMM/PBSA method

Identifiers

PMID27070572
PMCPMC4848968

What OpenQuestion holds

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Registered trials

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Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.